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SAB4200805

Sigma-Aldrich

Anti-β-Galactosidase antibody, Mouse monoclonal

clone GAL-13, purified from hybridoma cell culture

Synonyme(s) :

Anti-Beta-gal, Anti-Beta-galactosidase, Anti-Lactase

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Forme d'anticorps

purified from hybridoma cell culture

Type de produit anticorps

primary antibodies

Clone

GAL-13, monoclonal

Description

Research area: Microbiome

Forme

buffered aqueous solution

Espèces réactives

E. coli

Conditionnement

antibody small pack of 25 μL

Concentration

~1.0 mg/mL

Technique(s)

immunofluorescence: suitable
immunohistochemistry: suitable
indirect ELISA: 0.5-1 μg/mL using anti-Mouse antibody for coating, primary Anti-Beta-GAL antibody followed by addition of β-d-galactosidase enzyme from E. coli and 2-Nitrophenyl β-D-galactopyranoside as substrate.

Isotype

IgG1

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

Escherichia coli K12 ... Lacz(945006)

Description générale

Anti-nitric oxide synthase, inducible antibody, mouse monoclonal (mouse IgG1 isotype) is derived from the NOS-IN hybridoma, produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mouse immunized with a synthetic peptide corresponding to the C terminal region of nitric oxide synthase (NOS) of mouse macrophage origin (iNOS, also termed macNOS), conjugated to KLH
Beta galactosidases have been obtained from microorganisms such as fungi, bacteria and yeasts; plants, animals cells and from recombinant sources. This enzyme has two main applications; the removal of lactose from milk products for lactose intolerant people and the production of galactosylated products.Monoclonal Anti-Beta-Galactosidase recognizes soluble Beta-d-galactosidase and retains the enzymatic activity. The antibody reacts with the native enzyme and does not recognize denatured or reduced Beta-galactosidase. The Anti-Beta-Galactosidase antibody maybe useful tool for immunoenzymatic staining of blood and bone marrow smears or tissue sections. In addition, this product may be used as a primary antibody for the detection and purification of recombinant fusion hybrid proteins, which contain Beta-galactosidase (lacZ) in the cloning vector.

Immunogène

Beta-D-Galactosidase purified from E. coli

Application

Anti-Nitric Oxide Synthase, Inducible antibody, Mouse monoclonal has been used in: immunoblotting immunofluorescence fluorescence-activated cell sorting 3 (FACS3) immunohistochemistry
The antibody is recommended to use in various immunological techniques, including ELISA, Immunofluorescence and immunohistology.

Actions biochimiques/physiologiques

NO is a messenger molecule mediating diverse functions including vasodilatation, neurotransmission, antimicrobial and anti-tumor activities. It is implicated as a pathogenic mediator in a variety of conditions, including central nervous system (CNS) disease states, such as the animal model of multiple sclerosis (MS) and experimental allergic encephalomyelitis.

Forme physique

Supplied as a solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide as a preservative.

Autres remarques

This product is for R&D use only, not for drug, household, or other uses.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Anjali Bajpai et al.
Developmental biology, 457(1), 1-8 (2019-09-27)
The Hedgehog (Hh) morphogen regulates growth and patterning. Since Hh signaling is also implicated in carcinogenesis, it is conceivable that de novo Hh-secreting organizers, if formed in association with oncogenic hit could be tumor-cooperative. Here we validate this hypothesis using
Nitric oxide release: Part II
Carpenter AW and Mark HS
Chemical Society Reviews, 41(10), 3742-3752 (2012)

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